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Volumn 32, Issue 10, 2010, Pages 1449-1455

Tunicamycin inhibition of N-glycosylation of α-glucosidase from Aspergillus niveus: Partial influence on biochemical properties

Author keywords

glucosidase; Aspergillus niveus; N glycans; O glycans; Tunicamycin

Indexed keywords

ASPERGILLUS NIVEUS; GLUCOSIDASE; N-GLYCANS; O-GLYCANS; TUNICAMYCIN;

EID: 77956871306     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-010-0304-y     Document Type: Article
Times cited : (8)

References (23)
  • 1
    • 0020713174 scopus 로고
    • Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes
    • Bause E (1983) Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem J 209: 331-336.
    • (1983) Biochem J , vol.209 , pp. 331-336
    • Bause, E.1
  • 2
    • 0034072923 scopus 로고    scopus 로고
    • Glucoamylase activity from the thermophilic fungus Scytalidium thermophilum. Biochemical and regulatory properties
    • Cereia M, Terenzi HF, Jorge JA, Greene LJ, Rosa JC, Polizeli MLTM (2000) Glucoamylase activity from the thermophilic fungus Scytalidium thermophilum. Biochemical and regulatory properties. J Basic Microbiol 40(2): 83-92.
    • (2000) J Basic Microbiol , vol.40 , Issue.2 , pp. 83-92
    • Cereia, M.1    Terenzi, H.F.2    Jorge, J.A.3    Greene, L.J.4    Rosa, J.C.5    Polizeli, M.L.T.M.6
  • 4
    • 2942674460 scopus 로고    scopus 로고
    • Effect of adding and removing N-glycosylation recognition sites on the thermostability of barley α-glucosidase
    • Clark SE, Muslin EH, Henson CA (2004) Effect of adding and removing N-glycosylation recognition sites on the thermostability of barley α-glucosidase. Protein Eng Des Sel 17: 245-249.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 245-249
    • Clark, S.E.1    Muslin, E.H.2    Henson, C.A.3
  • 5
    • 0023159808 scopus 로고
    • Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains
    • Elbein AD (1987) Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Ann Rev Biochem 56: 497-534.
    • (1987) Ann Rev Biochem , vol.56 , pp. 497-534
    • Elbein, A.D.1
  • 6
    • 13644267779 scopus 로고    scopus 로고
    • Effects of tunicamycin, mannosamine, and other inhibitors of glycoprotein processing on skeletal alkaline phosphatase in human osteoblast-like cells
    • Farley JR, Magnusson P (2005) Effects of tunicamycin, mannosamine, and other inhibitors of glycoprotein processing on skeletal alkaline phosphatase in human osteoblast-like cells. Calcif Tissue Int 76: 63-74.
    • (2005) Calcif Tissue Int , vol.76 , pp. 63-74
    • Farley, J.R.1    Magnusson, P.2
  • 7
    • 77956883336 scopus 로고    scopus 로고
    • Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins MR, Appel RD, Bairoch A (2005) Protein identification and analysis tools on the ExPASy server. In: Walker JM (ed): The proteomics protocols handbook. Humana Press, Totowa, pp 571-607.
  • 8
    • 34347327263 scopus 로고    scopus 로고
    • Protein O-glycosylation in fungi: Diverse structures and multiple functions
    • Goto M (2007) Protein O-glycosylation in fungi: diverse structures and multiple functions. Biosci Biotechnol Biochem 71(6): 1415-1427.
    • (2007) Biosci Biotechnol Biochem , vol.71 , Issue.6 , pp. 1415-1427
    • Goto, M.1
  • 9
    • 0025045974 scopus 로고
    • Lectin affinity chromatography of proteins bearing O-linked oligosaccharides: Application of jacalin-agarose
    • Hortin GL, Trimpe BL (1990) Lectin affinity chromatography of proteins bearing O-linked oligosaccharides: application of jacalin-agarose. Anal Biochem 188(2): 271-277.
    • (1990) Anal Biochem , vol.188 , Issue.2 , pp. 271-277
    • Hortin, G.L.1    Trimpe, B.L.2
  • 10
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites
    • Julenius K, Molgaard A, Gupta R, Brunak S (2005) Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology 15: 153-164.
    • (2005) Glycobiology , vol.15 , pp. 153-164
    • Julenius, K.1    Molgaard, A.2    Gupta, R.3    Brunak, S.4
  • 11
    • 0017146754 scopus 로고
    • The structural basis of the different affinities of two types acidic N-glycosidic glycopeptides for concanavalin A-sepharose
    • Krusius T, Finne J, Rauvala H (1976) The structural basis of the different affinities of two types acidic N-glycosidic glycopeptides for concanavalin A-sepharose. FEBS Lett 72(1): 117-120.
    • (1976) FEBS Lett , vol.72 , Issue.1 , pp. 117-120
    • Krusius, T.1    Finne, J.2    Rauvala, H.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0343373949 scopus 로고
    • Enzyplot: A microcomputer assistant program for teaching enzyme kinetics
    • Leone FA, Baranauskas JA, Ciancaglini P (1995) Enzyplot: a microcomputer assistant program for teaching enzyme kinetics. Biochem Educ 23: 35-37.
    • (1995) Biochem Educ , vol.23 , pp. 35-37
    • Leone, F.A.1    Baranauskas, J.A.2    Ciancaglini, P.3
  • 14
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: Recent updates and new developments
    • Letunic I, Doerks T, Bork P (2009) SMART 6: recent updates and new developments. Nucl Acids Res 37: 229-232.
    • (2009) Nucl Acids Res , vol.37 , pp. 229-232
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 15
    • 0036184149 scopus 로고    scopus 로고
    • The effect of proline insertions on the thermostability of a barley alpha-glucosidase
    • Muslin EH, Clark SE, Henson CA (2002) The effect of proline insertions on the thermostability of a barley alpha-glucosidase. Protein Eng 15(1): 29-33.
    • (2002) Protein Eng , vol.15 , Issue.1 , pp. 29-33
    • Muslin, E.H.1    Clark, S.E.2    Henson, C.A.3
  • 16
    • 0016772320 scopus 로고
    • Fractionation of glycopeptides by affinity column chromatography on concanavalin A-sepharose
    • Ogata S, Muramatsu T, Kobata A (1975) Fractionation of glycopeptides by affinity column chromatography on concanavalin A-sepharose. J Biochem 78(4): 687-696.
    • (1975) J Biochem , vol.78 , Issue.4 , pp. 687-696
    • Ogata, S.1    Muramatsu, T.2    Kobata, A.3
  • 17
    • 12944323169 scopus 로고    scopus 로고
    • The effect of nitrogen source on yield and glycosylation of a human cystatin C mutant expressed in Pichia pastoris
    • Pritchett J, Baldwin SA (2004) The effect of nitrogen source on yield and glycosylation of a human cystatin C mutant expressed in Pichia pastoris. J Ind Microbiol Biotechnol 31: 553-558.
    • (2004) J Ind Microbiol Biotechnol , vol.31 , pp. 553-558
    • Pritchett, J.1    Baldwin, S.A.2
  • 18
    • 0021999231 scopus 로고
    • Jacalin: An IgA-binding lectin
    • Roque-Barreira MC, Campos Neto A (1985) Jacalin: An IgA-binding lectin. J Immunol 134: 1740-1743.
    • (1985) J Immunol , vol.134 , pp. 1740-1743
    • Roque-Barreira, M.C.1    Campos, N.A.2
  • 20
    • 63149160691 scopus 로고    scopus 로고
    • The effect of individual N-Glycans on enzyme activity
    • Skropeta D (2009) The effect of individual N-Glycans on enzyme activity. Bioorg Med Chem 17(2): 2645-2653.
    • (2009) Bioorg Med Chem , vol.17 , Issue.2 , pp. 2645-2653
    • Skropeta, D.1
  • 21
    • 0019850170 scopus 로고
    • The effect of tunicamycin on secreted glycosidases of Aspergillus niger
    • Speake BK, Malley DJ, Hemming FW (1981) The effect of tunicamycin on secreted glycosidases of Aspergillus niger. Arch Biochem Biophys 210: 110-117.
    • (1981) Arch Biochem Biophys , vol.210 , pp. 110-117
    • Speake, B.K.1    Malley, D.J.2    Hemming, F.W.3
  • 22
    • 0035801869 scopus 로고    scopus 로고
    • Effect of tunicamycin on N-acetil-β-D-glucosaminidase produced by Trichoderma harzianum
    • Ulhoa CJ, Sankievicz D, Limeira PS, Peberdy JF (2001) Effect of tunicamycin on N-acetil-β-D-glucosaminidase produced by Trichoderma harzianum. Biochim Biophys Acta 1528: 39-42.
    • (2001) Biochim Biophys Acta , vol.1528 , pp. 39-42
    • Ulhoa, C.J.1    Sankievicz, D.2    Limeira, P.S.3    Peberdy, J.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.